Evidence map›Paper›PMID 16194242›Full record

ArticleMolecular microbiology2005

Evidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK.

Brett Geissler, William Margolin

Abstract read
In one paragraph

Article in Molecular microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

76 citing papers in PubMed.

  1. iScience · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. FtsA acts through FtsW to promote cell wall synthesis during cell division inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Disruption of divisome assembly rescued by FtsN-FtsA interaction inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article

16 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Brett GeisslerDepartment of Microbiology and Molecular Genetics, University of Texas Medical School, 6431 Fannin, Houston, TX 77030, USA.
William Margolin

Funding

Targeting and assembly of E. coli division proteinsR01GM061074 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MARGOLIN, WILLIAM · 2000 to 2018
$5.7M
NIGMS NIH HHS R01 GM061074NIGMS NIH HHS R01-GM61074
6 · The paper itself

Abstract

In Escherichia coli, at least 12 proteins colocalize to the cell midpoint, assembling into a membrane-associated protein machine that forms the division septum. Many of these proteins, including FtsK, are essential for viability but their functions in cell division are unknown. Here we show that the essential function of FtsK in cell division can be partially bypassed. Cells containing either the ftsA R286W mutation or a plasmid carrying the ftsQAZ genes suppressed a ftsK44(ts) allele efficiently. Moreover, ftsA R286W or multicopy ftsQAZ, which can largely bypass the requirement for the essential cell division gene zipA, allowed cells with a complete deletion of ftsK to survive and divide, although many of these ftsK null cells formed multiseptate chains. Green fluorescent protein (GFP) fusions to FtsI and FtsN, which normally depend on FtsK to localize to division sites, localized to division sites in the absence of FtsK, indicating that FtsK is not directly involved in their recruitment. Cells expressing additional ftsQ, and to a lesser extent ftsB and ftsN, were able to survive and divide in the absence of ftsK, although cell chains were often formed. Surprisingly, the cytoplasmic and transmembrane domains of FtsQ, while not sufficient to complement an ftsQ null mutant, conferred viability and septum formation in the absence of ftsK. These findings suggest that the N-terminal domain of FtsK is normally involved in stability of the division protein machine and shares functional overlap with FtsQ, FtsB, FtsA, ZipA and FtsN.

Indexed as

Cell Cycle ProteinsCell DivisionCell ShapeCell SurvivalEscherichia coliEscherichia coli ProteinsGenetic Complementation TestMembrane ProteinsProtein Structure, TertiaryTemperatureCell Cycle ProteinsEscherichia coli ProteinsFtsK protein, E coliMembrane Proteins

Identifiers

PMID16194242
PMCPMC4758208

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.